Diacylglycerol kinases (DGKs) phosphorylate the neutral lipid diacylglycerol (DG) to produce phosphatidic acid (PA). In mammalian systems DGKs are a complex family of at least nine isoforms that are thought to participate in down-regulation of DG-based signalling pathways and perhaps activation of PA-stimulated signalling events. We report here that the simple protozoan amoeba Dictyostelium discoideum appears to contain a single gene encoding a DGK enzyme. This gene, dgkA, encodes a deduced protein that contains three C1-type cysteine-rich repeats, a DGK catalytic domain most closely related to the θ subtype of mammalian DGKs and a C-terminal segment containing a proline/glutamine-rich region and a large aspargine-repeat region. This gene corresponds to a previously reported myosin II heavy chain kinase designated myosin heavy chain-protein kinase C (MHC-PKC), but our analysis clearly demonstrates that this protein does not, as suggested by earlier data, contain a protein kinase catalytic domain. A FLAG-tagged version of DgkA expressed in Dictyostelium displayed robust DGK activity. Earlier studies indicating that disruption of this locus alters myosin II assembly levels in Dictyostelium raise the intriguing possibility that DG and/or PA metabolism may play a role in controlling myosin II assembly in this system.
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December 2002
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Research Article|
December 15 2002
Dictyostelium discoideum has a single diacylglycerol kinase gene with similarity to mammalian θ isoforms
Marc A. de la ROCHE;
Marc A. de la ROCHE
∗Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6
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Janet L. SMITH;
Janet L. SMITH
†Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472-2829, U.S.A.
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Maribel RICO;
Maribel RICO
‡Department of Physiology and Biophysics, Case Western Reserve School of Medicine, Cleveland, OH 44016-4970, U.S.A.,
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Silvia CARRASCO;
Silvia CARRASCO
§Department of Immunology and Oncology, National Center for Biotechnology, Campus de Cantoblanco, Madrid 28049, Spain
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Isabel MERIDA;
Isabel MERIDA
§Department of Immunology and Oncology, National Center for Biotechnology, Campus de Cantoblanco, Madrid 28049, Spain
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Lucila LICATE;
Lucila LICATE
‡Department of Physiology and Biophysics, Case Western Reserve School of Medicine, Cleveland, OH 44016-4970, U.S.A.,
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Graham P. CÔTÉ;
Graham P. CÔTÉ
∗Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6
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Thomas T. EGELHOFF
Thomas T. EGELHOFF
1
‡Department of Physiology and Biophysics, Case Western Reserve School of Medicine, Cleveland, OH 44016-4970, U.S.A.,
1To whom correspondence should be addressed (e-mail [email protected]).
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Publisher: Portland Press Ltd
Received:
July 01 2002
Revision Received:
September 20 2002
Accepted:
September 24 2002
Accepted Manuscript online:
September 24 2002
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2002
2002
Biochem J (2002) 368 (3): 809–815.
Article history
Received:
July 01 2002
Revision Received:
September 20 2002
Accepted:
September 24 2002
Accepted Manuscript online:
September 24 2002
Citation
Marc A. de la ROCHE, Janet L. SMITH, Maribel RICO, Silvia CARRASCO, Isabel MERIDA, Lucila LICATE, Graham P. CÔTÉ, Thomas T. EGELHOFF; Dictyostelium discoideum has a single diacylglycerol kinase gene with similarity to mammalian θ isoforms. Biochem J 15 December 2002; 368 (3): 809–815. doi: https://doi.org/10.1042/bj20021027
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